S4A8_HUMAN
ID S4A8_HUMAN Reviewed; 1093 AA.
AC Q2Y0W8; A0MMZ1; B4DHY0; E7EML0; F5GZ31; F5H7F5; O94843; O95233; Q004B4;
AC Q8N3U2; Q8TC60; Q9UKX8;
DT 08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Electroneutral sodium bicarbonate exchanger 1;
DE AltName: Full=Electroneutral Na(+)-driven Cl-HCO3 exchanger;
DE AltName: Full=Solute carrier family 4 member 8;
DE AltName: Full=k-NBC3;
GN Name=SLC4A8 {ECO:0000312|EMBL:AAY79176.1, ECO:0000312|HGNC:HGNC:11034};
GN Synonyms=KIAA0739, NBC {ECO:0000312|EMBL:AAC82380.1},
GN NBC3 {ECO:0000303|PubMed:10362779}, NDCBE1 {ECO:0000303|PubMed:11133997};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC82380.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, AND
RP INHIBITION.
RC TISSUE=Frontal cortex {ECO:0000312|EMBL:AAC82380.1};
RX PubMed=11133997; DOI=10.1074/jbc.c000716200;
RA Grichtchenko I.I., Choi I., Zhong X., Bray-Ward P., Russell J.M.,
RA Boron W.F.;
RT "Cloning, characterization, and chromosomal mapping of a human
RT electroneutral Na(+)-driven Cl-HCO3 exchanger.";
RL J. Biol. Chem. 276:8358-8363(2001).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAY79176.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 4 AND 5).
RC TISSUE=Brain {ECO:0000312|EMBL:AAY79176.1}, and
RC Heart {ECO:0000312|EMBL:ABJ91577.1};
RA Bouyer P., Parker M.D., Boron W.F.;
RT "An electroneutral Na+-driven Cl-HCO3 exchanger (NDCBE1) with a novel COOH-
RT terminus cloned from human brain.";
RL Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAA34459.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain {ECO:0000312|EMBL:BAA34459.1};
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8).
RC TISSUE=Caudate nucleus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 7).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [7] {ECO:0000305, ECO:0000312|EMBL:AAY79176.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8] {ECO:0000305, ECO:0000312|EMBL:AAH25994.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Testis {ECO:0000312|EMBL:AAH25994.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9] {ECO:0000305, ECO:0000312|EMBL:AAD52981.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-670 (ISOFORMS 1/3/6), FUNCTION, TISSUE
RP SPECIFICITY, AND INHIBITION.
RC TISSUE=Testis carcinoma {ECO:0000269|PubMed:10362779};
RX PubMed=10362779; DOI=10.1152/ajprenal.1999.276.6.f903;
RA Amlal H., Burnham C.E., Soleimani M.;
RT "Characterization of Na+/HCO-3 cotransporter isoform NBC-3.";
RL Am. J. Physiol. 276:F903-F913(1999).
RN [10]
RP ERRATUM OF PUBMED:10362779.
RA Amlal H., Burnham C.E., Soleimani M.;
RL Am. J. Physiol. 277:F477-F477(1999).
RN [11] {ECO:0000305}
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17715183; DOI=10.1152/ajpregu.00356.2007;
RA Damkier H.H., Nielsen S., Praetorius J.;
RT "Molecular expression of SLC4-derived Na+-dependent anion transporters in
RT selected human tissues.";
RL Am. J. Physiol. 293:R2136-R2146(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
CC -!- FUNCTION: Mediates electroneutral sodium- and carbonate-dependent
CC chloride-HCO3(-) exchange with a Na(+):HCO3(-) stoichiometry of 2:1.
CC Plays a major role in pH regulation in neurons. May be involved in cell
CC pH regulation by transporting HCO3(-) from blood to cell. Enhanced
CC expression in severe acid stress could be important for cell survival
CC by mediating the influx of HCO3(-) into the cells. Also mediates
CC lithium-dependent HCO3(-) cotransport. May be regulated by osmolarity.
CC {ECO:0000269|PubMed:10362779, ECO:0000269|PubMed:11133997}.
CC -!- ACTIVITY REGULATION: Activity is inhibited by 4,4'-Di-
CC isothiocyanatostilbene-2,2'-disulfonic acid (DIDS - an inhibitor of
CC several anion channels and transporters).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:17715183}; Multi-
CC pass membrane protein {ECO:0000269|PubMed:17715183}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=1 {ECO:0000269|Ref.2};
CC IsoId=Q2Y0W8-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:9872452};
CC IsoId=Q2Y0W8-2; Sequence=VSP_052760, VSP_052765;
CC Name=3 {ECO:0000269|PubMed:11133997};
CC IsoId=Q2Y0W8-3; Sequence=VSP_052765;
CC Name=4 {ECO:0000269|Ref.2};
CC IsoId=Q2Y0W8-4; Sequence=VSP_052759, VSP_052765;
CC Name=5 {ECO:0000269|Ref.2};
CC IsoId=Q2Y0W8-5; Sequence=VSP_052759;
CC Name=6 {ECO:0000269|PubMed:15489334};
CC IsoId=Q2Y0W8-6; Sequence=VSP_052761, VSP_052762;
CC Name=7;
CC IsoId=Q2Y0W8-7; Sequence=VSP_052759, VSP_052763, VSP_052764;
CC Name=8;
CC IsoId=Q2Y0W8-8; Sequence=VSP_052759, VSP_052761, VSP_052762;
CC -!- TISSUE SPECIFICITY: Expressed in the pyramidal cells of the hippocampus
CC (at protein level). Highly expressed in all major regions of the brain,
CC spinal column and in testis, and moderate levels in trachea, thyroid
CC and medulla region of kidney. Low expression levels observed in
CC pancreas and kidney cortex. {ECO:0000269|PubMed:10362779,
CC ECO:0000269|PubMed:11133997, ECO:0000269|PubMed:17715183}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 4]: May be due to an intron retention.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the anion exchanger (TC 2.A.31) family.
CC {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA34459.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD38576.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF069512; AAC82380.1; -; mRNA.
DR EMBL; DQ063579; AAY79176.1; -; mRNA.
DR EMBL; DQ975204; ABJ09587.1; -; mRNA.
DR EMBL; DQ996537; ABJ91576.1; -; mRNA.
DR EMBL; DQ996398; ABJ91577.1; -; mRNA.
DR EMBL; AB018282; BAA34459.1; ALT_INIT; mRNA.
DR EMBL; AK295315; BAG58292.1; -; mRNA.
DR EMBL; AL831915; CAD38576.2; ALT_INIT; mRNA.
DR EMBL; AC025097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC046135; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW58192.1; -; Genomic_DNA.
DR EMBL; BC025994; AAH25994.1; -; mRNA.
DR EMBL; AF107099; AAD52981.1; -; mRNA.
DR CCDS; CCDS44890.1; -. [Q2Y0W8-1]
DR CCDS; CCDS58232.1; -. [Q2Y0W8-7]
DR CCDS; CCDS58233.1; -. [Q2Y0W8-8]
DR CCDS; CCDS73470.1; -. [Q2Y0W8-5]
DR RefSeq; NP_001035049.1; NM_001039960.2. [Q2Y0W8-1]
DR RefSeq; NP_001245330.1; NM_001258401.2. [Q2Y0W8-5]
DR RefSeq; NP_001245331.1; NM_001258402.1. [Q2Y0W8-6]
DR RefSeq; NP_001245332.1; NM_001258403.1. [Q2Y0W8-7]
DR RefSeq; NP_001254544.1; NM_001267615.1. [Q2Y0W8-8]
DR RefSeq; XP_016875730.1; XM_017020241.1. [Q2Y0W8-2]
DR PDB; 5JHO; X-ray; 2.80 A; A/B=54-397.
DR PDBsum; 5JHO; -.
DR AlphaFoldDB; Q2Y0W8; -.
DR SMR; Q2Y0W8; -.
DR BioGRID; 114877; 34.
DR IntAct; Q2Y0W8; 30.
DR STRING; 9606.ENSP00000405812; -.
DR DrugBank; DB01390; Sodium bicarbonate.
DR TCDB; 2.A.31.2.4; the anion exchanger (ae) family.
DR iPTMnet; Q2Y0W8; -.
DR PhosphoSitePlus; Q2Y0W8; -.
DR SwissPalm; Q2Y0W8; -.
DR BioMuta; SLC4A8; -.
DR DMDM; 121942008; -.
DR EPD; Q2Y0W8; -.
DR jPOST; Q2Y0W8; -.
DR MassIVE; Q2Y0W8; -.
DR MaxQB; Q2Y0W8; -.
DR PaxDb; Q2Y0W8; -.
DR PeptideAtlas; Q2Y0W8; -.
DR PRIDE; Q2Y0W8; -.
DR ProteomicsDB; 16963; -.
DR ProteomicsDB; 24921; -.
DR ProteomicsDB; 61540; -. [Q2Y0W8-1]
DR ProteomicsDB; 61541; -. [Q2Y0W8-2]
DR ProteomicsDB; 61542; -. [Q2Y0W8-3]
DR ProteomicsDB; 61543; -. [Q2Y0W8-4]
DR ProteomicsDB; 61544; -. [Q2Y0W8-5]
DR ProteomicsDB; 61545; -. [Q2Y0W8-6]
DR ProteomicsDB; 61546; -. [Q2Y0W8-7]
DR Antibodypedia; 26410; 177 antibodies from 25 providers.
DR DNASU; 9498; -.
DR Ensembl; ENST00000358657.7; ENSP00000351483.4; ENSG00000050438.17. [Q2Y0W8-5]
DR Ensembl; ENST00000453097.7; ENSP00000405812.2; ENSG00000050438.17. [Q2Y0W8-1]
DR Ensembl; ENST00000514353.7; ENSP00000442561.2; ENSG00000050438.17. [Q2Y0W8-7]
DR Ensembl; ENST00000535225.6; ENSP00000441520.1; ENSG00000050438.17. [Q2Y0W8-8]
DR GeneID; 9498; -.
DR KEGG; hsa:9498; -.
DR MANE-Select; ENST00000453097.7; ENSP00000405812.2; NM_001039960.3; NP_001035049.1.
DR UCSC; uc001rys.3; human. [Q2Y0W8-1]
DR CTD; 9498; -.
DR DisGeNET; 9498; -.
DR GeneCards; SLC4A8; -.
DR HGNC; HGNC:11034; SLC4A8.
DR HPA; ENSG00000050438; Group enriched (brain, pituitary gland, retina, testis).
DR MIM; 605024; gene.
DR neXtProt; NX_Q2Y0W8; -.
DR OpenTargets; ENSG00000050438; -.
DR PharmGKB; PA35900; -.
DR VEuPathDB; HostDB:ENSG00000050438; -.
DR eggNOG; KOG1172; Eukaryota.
DR GeneTree; ENSGT00940000157422; -.
DR HOGENOM; CLU_002289_5_3_1; -.
DR InParanoid; Q2Y0W8; -.
DR OMA; VCHIEAE; -.
DR OrthoDB; 265068at2759; -.
DR PhylomeDB; Q2Y0W8; -.
DR TreeFam; TF313630; -.
DR PathwayCommons; Q2Y0W8; -.
DR Reactome; R-HSA-425381; Bicarbonate transporters.
DR SignaLink; Q2Y0W8; -.
DR SIGNOR; Q2Y0W8; -.
DR BioGRID-ORCS; 9498; 17 hits in 1072 CRISPR screens.
DR ChiTaRS; SLC4A8; human.
DR GeneWiki; SLC4A8; -.
DR GenomeRNAi; 9498; -.
DR Pharos; Q2Y0W8; Tbio.
DR PRO; PR:Q2Y0W8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q2Y0W8; protein.
DR Bgee; ENSG00000050438; Expressed in pons and 166 other tissues.
DR Genevisible; Q2Y0W8; HS.
DR GO; GO:0032279; C:asymmetric synapse; ISS:ARUK-UCL.
DR GO; GO:0043679; C:axon terminus; ISS:ARUK-UCL.
DR GO; GO:0030425; C:dendrite; IDA:ARUK-UCL.
DR GO; GO:0097386; C:glial cell projection; ISS:ARUK-UCL.
DR GO; GO:0098978; C:glutamatergic synapse; ISS:ARUK-UCL.
DR GO; GO:0097457; C:hippocampal mossy fiber; ISS:ARUK-UCL.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; ISS:ARUK-UCL.
DR GO; GO:0043005; C:neuron projection; ISS:ARUK-UCL.
DR GO; GO:0032809; C:neuronal cell body membrane; ISS:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0098793; C:presynapse; ISS:ARUK-UCL.
DR GO; GO:0042734; C:presynaptic membrane; ISS:ARUK-UCL.
DR GO; GO:0032280; C:symmetric synapse; ISS:ARUK-UCL.
DR GO; GO:0008021; C:synaptic vesicle; ISS:ARUK-UCL.
DR GO; GO:0043195; C:terminal bouton; ISS:ARUK-UCL.
DR GO; GO:0015301; F:anion:anion antiporter activity; IEA:UniProtKB-KW.
DR GO; GO:0015106; F:bicarbonate transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0015108; F:chloride transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0005452; F:inorganic anion exchanger activity; TAS:Reactome.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:0008510; F:sodium:bicarbonate symporter activity; IDA:ARUK-UCL.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015701; P:bicarbonate transport; IDA:ARUK-UCL.
DR GO; GO:1902476; P:chloride transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0050801; P:ion homeostasis; IBA:GO_Central.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; ISS:ARUK-UCL.
DR GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; ISS:ARUK-UCL.
DR GO; GO:0051453; P:regulation of intracellular pH; IDA:ARUK-UCL.
DR GO; GO:0042391; P:regulation of membrane potential; IDA:ARUK-UCL.
DR GO; GO:0035725; P:sodium ion transmembrane transport; IDA:ARUK-UCL.
DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR Gene3D; 3.40.930.10; -; 1.
DR InterPro; IPR013769; Band3_cytoplasmic_dom.
DR InterPro; IPR011531; HCO3_transpt-like_TM_dom.
DR InterPro; IPR003020; HCO3_transpt_euk.
DR InterPro; IPR003024; Na/HCO3_transpt.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR PANTHER; PTHR11453; PTHR11453; 1.
DR Pfam; PF07565; Band_3_cyto; 1.
DR Pfam; PF00955; HCO3_cotransp; 1.
DR PRINTS; PR01231; HCO3TRNSPORT.
DR PRINTS; PR01232; NAHCO3TRSPRT.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00834; ae; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Anion exchange; Antiport; Coiled coil;
KW Disulfide bond; Ion transport; Membrane; Reference proteome; Sodium;
KW Sodium transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..1093
FT /note="Electroneutral sodium bicarbonate exchanger 1"
FT /id="PRO_0000328922"
FT TOPO_DOM 1..478
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 500..523
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..565
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 566..586
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 587..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 596..616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 617..687
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 688..708
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 709..731
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 732..752
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 753..778
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 779..799
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 800..824
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 825..845
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 846..881
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 882..902
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 903..904
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 905..925
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 926..962
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 963..983
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 984..1093
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 55..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1010..1036
FT /evidence="ECO:0000255"
FT COMPBIAS 57..77
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 636..638
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT DISULFID 672..684
FT /evidence="ECO:0000250|UniProtKB:Q9Y6R1"
FT VAR_SEQ 1..53
FT /note="Missing (in isoform 4, isoform 5, isoform 7 and
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2"
FT /id="VSP_052759"
FT VAR_SEQ 1..16
FT /note="MPAAGSNEPDGVLSYQ -> MFNKNNSNKLRSTPRYRRGDPGYLNFTELGPL
FT KPEQKDQWSQH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9872452"
FT /id="VSP_052760"
FT VAR_SEQ 671..691
FT /note="ECQEMHGEFMGSACGHHGPYT -> VSLGAARCPSIVTTGLGGTSK (in
FT isoform 6 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_052761"
FT VAR_SEQ 692..1093
FT /note="Missing (in isoform 6 and isoform 8)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_052762"
FT VAR_SEQ 725..800
FT /note="VRSMVSDFAVFLTIFTMVIIDFLIGVPSPKLQVPSVFKPTRDDRGWIINPIG
FT PNPWWTVIAAIIPALLCTILIFMD -> MESCSVAWLECGGVILAHCNLRLLPSSWDYR
FT HAPPQPANFCIFSRDGVSPCWPGWSQSLDLVICLPRPPKMLGLQA (in isoform
FT 7)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_052763"
FT VAR_SEQ 801..1093
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_052764"
FT VAR_SEQ 1028..1093
FT /note="EAEKMLEIGGDKFPLESRKLLSSPGKNISCRCDPSEINISDEMPKTTVWKAL
FT SMNSGNAKEKSLFN -> VIVLAPTVYLGASNYRT (in isoform 2, isoform
FT 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:11133997,
FT ECO:0000303|PubMed:9872452, ECO:0000303|Ref.2"
FT /id="VSP_052765"
FT VARIANT 312
FT /note="D -> A (in dbSNP:rs35966334)"
FT /id="VAR_048351"
FT VARIANT 898
FT /note="I -> V (in dbSNP:rs12318785)"
FT /id="VAR_048352"
FT CONFLICT 482
FT /note="F -> L (in Ref. 4; BAG58292)"
FT /evidence="ECO:0000305"
FT CONFLICT 1008
FT /note="M -> T (in Ref. 1; AAC82380)"
FT /evidence="ECO:0000305"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:5JHO"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:5JHO"
FT STRAND 133..147
FT /evidence="ECO:0007829|PDB:5JHO"
FT HELIX 148..150
FT /evidence="ECO:0007829|PDB:5JHO"
FT HELIX 163..175
FT /evidence="ECO:0007829|PDB:5JHO"
FT STRAND 176..182
FT /evidence="ECO:0007829|PDB:5JHO"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:5JHO"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:5JHO"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:5JHO"
FT HELIX 206..216
FT /evidence="ECO:0007829|PDB:5JHO"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:5JHO"
FT STRAND 299..308
FT /evidence="ECO:0007829|PDB:5JHO"
FT STRAND 315..325
FT /evidence="ECO:0007829|PDB:5JHO"
FT TURN 328..330
FT /evidence="ECO:0007829|PDB:5JHO"
FT STRAND 331..333
FT /evidence="ECO:0007829|PDB:5JHO"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:5JHO"
FT HELIX 350..363
FT /evidence="ECO:0007829|PDB:5JHO"
FT HELIX 367..375
FT /evidence="ECO:0007829|PDB:5JHO"
FT HELIX 379..392
FT /evidence="ECO:0007829|PDB:5JHO"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:5JHO"
FT CONFLICT Q2Y0W8-7:707
FT /note="Q -> R (in Ref. 5; CAD38576)"
FT /evidence="ECO:0000305"
FT CONFLICT Q2Y0W8-7:716
FT /note="R -> G (in Ref. 5; CAD38576)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1093 AA; 122938 MW; DDF9D0BC3CBD1A06 CRC64;
MPAAGSNEPD GVLSYQRPDE EAVVDQGGTS TILNIHYEKE ELEGHRTLYV GVRMPLGRQS
HRHHRTHGQK HRRRGRGKGA SQGEEGLEAL AHDTPSQRVQ FILGTEEDEE HVPHELFTEL
DEICMKEGED AEWKETARWL KFEEDVEDGG ERWSKPYVAT LSLHSLFELR SCLINGTVLL
DMHANSIEEI SDLILDQQEL SSDLNDSMRV KVREALLKKH HHQNEKKRNN LIPIVRSFAE
VGKKQSDPHL MDKHGQTVSP QSVPTTNLEV KNGVNCEHSP VDLSKVDLHF MKKIPTGAEA
SNVLVGEVDI LDRPIVAFVR LSPAVLLSGL TEVPIPTRFL FILLGPVGKG QQYHEIGRSM
ATIMTDEIFH DVAYKAKERD DLLAGIDEFL DQVTVLPPGE WDPSIRIEPP KNVPSQEKRK
MPGVPNGNVC HIEQEPHGGH SGPELQRTGR LFGGLVLDIK RKAPWYWSDY RDALSLQCLA
SFLFLYCACM SPVITFGGLL GEATEGRISA IESLFGASMT GIAYSLFAGQ ALTILGSTGP
VLVFEKILFK FCKDYALSYL SLRACIGLWT AFLCIVLVAT DASSLVCYIT RFTEEAFASL
ICIIFIYEAI EKLIHLAETY PIHMHSQLDH LSLYYCRCTL PENPNNHTLQ YWKDHNIVTA
EVHWANLTVS ECQEMHGEFM GSACGHHGPY TPDVLFWSCI LFFTTFILSS TLKTFKTSRY
FPTRVRSMVS DFAVFLTIFT MVIIDFLIGV PSPKLQVPSV FKPTRDDRGW IINPIGPNPW
WTVIAAIIPA LLCTILIFMD QQITAVIINR KEHKLKKGCG YHLDLLMVAI MLGVCSIMGL
PWFVAATVLS ITHVNSLKLE SECSAPGEQP KFLGIREQRV TGLMIFVLMG CSVFMTAILK
FIPMPVLYGV FLYMGVSSLQ GIQFFDRLKL FGMPAKHQPD FIYLRHVPLR KVHLFTLIQL
TCLVLLWVIK ASPAAIVFPM MVLALVFVRK VMDLCFSKRE LSWLDDLMPE SKKKKLDDAK
KKAKEEEEAE KMLEIGGDKF PLESRKLLSS PGKNISCRCD PSEINISDEM PKTTVWKALS
MNSGNAKEKS LFN
